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Lookup NU author(s): Dr James StachORCiD
This is the authors' accepted manuscript of an article that has been published in its final definitive form by Wiley Blackwell, 2019.
For re-use rights please refer to the publisher's terms and conditions.
© 2019 Wiley-VCH Verlag GmbH & Co. KGaA, WeinheimCarbon-carbon bond formation is a fundamental transformation in both synthetic chemistry and biosynthesis. Enzymes catalyze such reactions with exquisite selectivity which often cannot be achieved using non-biological methods but may suffer from an intolerance of high temperature and the presence of organic solvents limiting their applications. Here we report the thermodynamic and kinetic stability of the β-barrel natural Diels-Alderase AbyU, which catalyzes formation of the spirotetronate core of the antimicrobial natural product abyssomicin C, with creation of 3 new asymmetric centers. This enzyme is shown to catalyze [4+2] cycloadditions at elevated temperature (up to 65 °C), and in the presence of organic solvents (MeOH, CH3CN and DMSO) and the chemical denaturant guanidinium hydrochloride, revealing that AbyU has potential widespread value as a biocatalyst.
Author(s): Marsh CO, Lees NR, Han L-C, Byrne MJ, Mbatha SZ, Maschio L, Pagden-Ratcliffe S, Duke PW, Stach JEM, Curnow P, Willis CL, Race PR
Publication type: Article
Publication status: Published
Print publication date: 01/10/2019
Online publication date: 25/08/2019
Acceptance date: 21/08/2019
Date deposited: 07/11/2019
ISSN (print): 1867-3880
ISSN (electronic): 1867-3899
Publisher: Wiley Blackwell
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